MYO10_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYO10_MOUSE
• UniProt AC: F8VQB6
• Protein Name: Unconventional myosin-X
• Gene Name: Myo10
• Organism: Mus musculus (Mouse).
• Sequence Length: 2062
• Subcellular Localization: Cytoplasm, cytosol. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein. May be in an inactive, m
• Protein Description: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments (By similarity). Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts.; Isoform Headless: Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion..
• Protein Sequence: MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLAELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEEYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQQTLDLGLQEKTSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQQGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVITAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQIPFKTALGRSADLLGLDPTQLTDALTQRSMILRGEEILTPLSVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNTQKMPDQFDQVVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPDDIRGKCTVLLQVYDASNSEWQLGKTKVFLRESLEQKLEKRREEEIDRAAMVIRAHILGYLARKQYRKVLCGVVTIQKNYRAFLARKKFLHLKKAAIVFQKQLRGQLARRVYRQLLAEKRELEEKKRREEEKKREEEERERERAQREADLLRAHQEAETRRQQELEALQKSQREADLTRELEKQRENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEISGEELSELAESASGEKPNFNFSQPYPAEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNYTVVPTSPSADSTVLLAASMQDSASLHNSSSGESTYCMPQNNGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRYSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTSKENGIDIILADRTFHLIAESPEDASQWFSVLSQVHSSTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGQVDKAIESRTIVADVLAKFEKLAATSEAGDAPWKFYFKLYCFLDTDSMPKDSVEFAFMFEQAHEAVIHGHHPAPEESLQVLAALRLQYLQGDYTPHTSIPPLEEVYSVQRLRARISQSTKTFTPYERLEKRRTSFLEGTLRRSFRTGSVVRQKAEEEQMLDMWIKEEVCSARTSIIDKWKKLQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGKPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSVSSQGSSR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDSFFPEG -------CCCCCCCC	42.52	-
585	Phosphorylation	ESRFDFIYDLFEHVS HCCCHHHHHHHHHHH	13.44	-
874	Phosphorylation	SQREADLTRELEKQR HHHHHHHHHHHHHHH	23.73	21183079
917	Ubiquitination	LTEASLQKLQQLRDE CCHHHHHHHHHHCHH	54.26	-
959	Phosphorylation	CVRNIERSLSVGSEI HHHHHHHHHCCCCCC	16.53	29550500
961	Phosphorylation	RNIERSLSVGSEISG HHHHHHHCCCCCCCH	26.19	26643407
964	Phosphorylation	ERSLSVGSEISGEEL HHHHCCCCCCCHHHH	29.60	26643407
967	Phosphorylation	LSVGSEISGEELSEL HCCCCCCCHHHHHHH	35.78	25195567
972	Phosphorylation	EISGEELSELAESAS CCCHHHHHHHHHHHC	33.57	29472430
1011	Phosphorylation	DDDAFKDSPNPSEHG CCCHHCCCCCCCCCC	27.45	29550500
1015	Phosphorylation	FKDSPNPSEHGHSDQ HCCCCCCCCCCCCCC	49.19	29550500
1020	Phosphorylation	NPSEHGHSDQRTSGI CCCCCCCCCCCCCCC	39.78	29550500
1024	Phosphorylation	HGHSDQRTSGIRTSD CCCCCCCCCCCCCCC	26.18	29472430
1025	Phosphorylation	GHSDQRTSGIRTSDD CCCCCCCCCCCCCCC	34.12	29472430
1127	Phosphorylation	QWSPDYRYSVGTYNS CCCCCEEEEEECCCC	11.07	25367039
1128	Phosphorylation	WSPDYRYSVGTYNSS CCCCEEEEEECCCCC	12.69	24899341
1131	Phosphorylation	DYRYSVGTYNSSGAY CEEEEEECCCCCCCE	19.85	26643407
1132	Phosphorylation	YRYSVGTYNSSGAYR EEEEEECCCCCCCEE	13.71	26032504
1134	Phosphorylation	YSVGTYNSSGAYRFS EEEECCCCCCCEECC	21.53	24899341
1135	Phosphorylation	SVGTYNSSGAYRFSS EEECCCCCCCEECCC	24.65	24899341
1138	Phosphorylation	TYNSSGAYRFSSEGA CCCCCCCEECCCCCC	18.73	26643407
1141	Phosphorylation	SSGAYRFSSEGAQSS CCCCEECCCCCCCCC	20.62	25293948
1142	Phosphorylation	SGAYRFSSEGAQSSF CCCEECCCCCCCCCC	37.02	25293948
1147	Phosphorylation	FSSEGAQSSFEDSEE CCCCCCCCCCCCCHH	36.14	25293948
1148	Phosphorylation	SSEGAQSSFEDSEED CCCCCCCCCCCCHHH	22.15	25293948
1152	Phosphorylation	AQSSFEDSEEDFDSR CCCCCCCCHHHHHHC	35.37	21149613
1162	Phosphorylation	DFDSRFDTDDELSYR HHHHCCCCCCCCCCC	42.51	21149613
1167	Phosphorylation	FDTDDELSYRRDSVY CCCCCCCCCCCCCHH	17.97	21743459
1172	Phosphorylation	ELSYRRDSVYSCVTL CCCCCCCCHHHHHHH	22.57	26643407
1174	Phosphorylation	SYRRDSVYSCVTLPY CCCCCCHHHHHHHHH	10.58	26643407
1175	Phosphorylation	YRRDSVYSCVTLPYF CCCCCHHHHHHHHHH	10.43	26643407
1195	Phosphorylation	MKGGLMNSWKRRWCV HCCCCCCCCEEEEEE	21.73	-
1234	Phosphorylation	GGGSSTLSRRNWKKR CCCCCCCCCCHHHHH	29.31	23140645
1257	Phosphorylation	LMYFENDSEEKLKGT EEEEECCCHHHHCCE	60.27	27357545
1277	Phosphorylation	AKEIIDNTSKENGID HHHHHHCCCHHHCEE	37.11	-
1278	Phosphorylation	KEIIDNTSKENGIDI HHHHHCCCHHHCEEE	44.20	-
1415	Phosphorylation	KNSPKMSSLKLKKRW CCCCCCCCCCCCCCE	26.48	29895711
1681	Acetylation	LFIYESLKKTKCREF HHHHHHHHCCCCCCC	68.61	15618613
1682	Acetylation	FIYESLKKTKCREFV HHHHHHHCCCCCCCC	59.52	8276657
1715	Phosphorylation	VYCHGGGSCKITINS EEECCCCEEEEEECC	18.60	25521595
1878	Phosphorylation	STKTFTPYERLEKRR CCCCCCHHHHHHHHH	15.60	20116462
1886	Phosphorylation	ERLEKRRTSFLEGTL HHHHHHHHCHHHHHH	28.06	24899341
1887	Phosphorylation	RLEKRRTSFLEGTLR HHHHHHHCHHHHHHH	26.48	26824392
1892	Phosphorylation	RTSFLEGTLRRSFRT HHCHHHHHHHHHHCC	14.02	23140645
2049	Phosphorylation	SMIVKKRYSTTRSVS HHHHHHCCCCCCCCC	21.17	21183079
2050	Phosphorylation	MIVKKRYSTTRSVSS HHHHHCCCCCCCCCC	27.60	21183079
2051	Phosphorylation	IVKKRYSTTRSVSSQ HHHHCCCCCCCCCCC	19.79	21183079

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MYO10_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MYO10_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MYO10_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of MYO10_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.